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2,6-dimethylheptanoyl-CoA is a specific substrate for long-chain acyl-CoA dehydrogenase (LCAD): evidence for a major role of LCAD in branched-chain fatty acid oxidation.

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Chicago
WANDERS, RJA, S DENIS, JPN RUITER, L IJLST, and Georges Dacremont. 1998. “2,6-dimethylheptanoyl-CoA Is a Specific Substrate for Long-chain acyl-CoA Dehydrogenase (LCAD): Evidence for a Major Role of LCAD in Branched-chain Fatty Acid Oxidation.” Biochimica Et Biophysica Acta-lipids and Lipid Metabolism 1393 (1): 35–40.
APA
WANDERS, R., DENIS, S., RUITER, J., IJLST, L., & Dacremont, G. (1998). 2,6-dimethylheptanoyl-CoA is a specific substrate for long-chain acyl-CoA dehydrogenase (LCAD): evidence for a major role of LCAD in branched-chain fatty acid oxidation. BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM, 1393(1), 35–40.
Vancouver
1.
WANDERS R, DENIS S, RUITER J, IJLST L, Dacremont G. 2,6-dimethylheptanoyl-CoA is a specific substrate for long-chain acyl-CoA dehydrogenase (LCAD): evidence for a major role of LCAD in branched-chain fatty acid oxidation. BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM. 1998;1393(1):35–40.
MLA
WANDERS, RJA, S DENIS, JPN RUITER, et al. “2,6-dimethylheptanoyl-CoA Is a Specific Substrate for Long-chain acyl-CoA Dehydrogenase (LCAD): Evidence for a Major Role of LCAD in Branched-chain Fatty Acid Oxidation.” BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM 1393.1 (1998): 35–40. Print.
@article{179533,
  author       = {WANDERS, RJA and DENIS, S and RUITER, JPN and IJLST, L and Dacremont, Georges},
  issn         = {0005-2760},
  journal      = {BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM},
  language     = {eng},
  number       = {1},
  pages        = {35--40},
  title        = {2,6-dimethylheptanoyl-CoA is a specific substrate for long-chain acyl-CoA dehydrogenase (LCAD): evidence for a major role of LCAD in branched-chain fatty acid oxidation.},
  volume       = {1393},
  year         = {1998},
}

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